scholarly journals The key DNA-binding residues in the C-terminal domain of Mycobacterium tuberculosis DNA gyrase A subunit (GyrA)

2006 ◽  
Vol 34 (19) ◽  
pp. 5650-5659 ◽  
Author(s):  
You-Yi Huang ◽  
Jiao-Yu Deng ◽  
Jing Gu ◽  
Zhi-Ping Zhang ◽  
Anthony Maxwell ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Dna Binding ◽  
Dna Gyrase ◽  
Terminal Domain ◽  
Gyrase A ◽  
A Subunit ◽  
Binding Residues

scholarly journals The pivot point arginines identified in the β-pinwheel structure of C-terminal domain from Salmonella Typhi DNA Gyrase A subunit

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Ekta Sachdeva ◽  
Gurpreet Kaur ◽  
Pragya Tiwari ◽  
Deepali Gupta ◽  
Tej P. Singh ◽  
...  
Keyword(s):  
Dna Gyrase ◽  
Salmonella Typhi ◽  
Pivot Point ◽  
Terminal Domain ◽  
Gyrase A ◽  
A Subunit

scholarly journals Disruption of the Borrelia burgdorferi gac Gene, Encoding the Naturally Synthesized GyrA C-Terminal Domain

2000 ◽  
Vol 182 (7) ◽  
pp. 2048-2051 ◽  
Author(s):  
Scott W. Knight ◽  
Betsy J. Kimmel ◽  
Christian H. Eggers ◽  
D. Scott Samuels
Keyword(s):  
Dna Binding ◽  
Borrelia Burgdorferi ◽  
Binding Protein ◽  
Dna Gyrase ◽  
Dna Binding Protein ◽  
Gene Encoding ◽  
Terminal Domain ◽  
A Subunit ◽  
Dna Maintenance ◽  
Independent Protein

ABSTRACT The C-terminal domain of the A subunit of DNA gyrase, which we term Gac, is naturally synthesized in Borrelia burgdorferi as an abundant DNA-binding protein. Full-length GyrA, which includes the C-terminal domain, is also synthesized by the spirochete and functions as a subunit of DNA gyrase. We have disrupted synthesis of Gac as an independent protein and demonstrated that it is not essential for growth in a coumarin-resistant background. We detected no alterations in DNA maintenance, condensation, or topology in B. burgdorferi lacking this small DNA-binding protein.

scholarly journals Mapping Simocyclinone D8 Interaction with DNA Gyrase: Evidence for a New Binding Site on GyrB

2009 ◽  
Vol 54 (1) ◽  
pp. 213-220 ◽  
Author(s):  
C. Sissi ◽  
E. Vazquez ◽  
A. Chemello ◽  
L. A. Mitchenall ◽  
A. Maxwell ◽  
...  
Keyword(s):  
Dna Gyrase ◽  
Coumarin Derivative ◽  
Streptomyces Antibioticus ◽  
B Subunit ◽  
Terminal Domain ◽  
Antiproliferative Agent ◽  
Gyrase A ◽  
A Subunit ◽  
The Individual ◽  
Simocyclinone D8

ABSTRACT Simocyclinone D8, a coumarin derivative isolated from Streptomyces antibioticus Tü 6040, represents an interesting new antiproliferative agent. It was originally suggested that this drug recognizes the GyrA subunit and interferes with the gyrase catalytic cycle by preventing its binding to DNA. To further characterize the mode of action of this antibiotic, we investigated its binding to the reconstituted DNA gyrase (A2B2) as well as to its GyrA and GyrB subunits and the individual domains of these proteins, by performing protein melting and proteolytic digestion studies as well as inhibition assays. Two binding sites were identified, one (anticipated) in the N-terminal domain of GyrA (GyrA59) and the other (unexpected) at the C-terminal domain of GyrB (GyrB47). Stabilization of the A subunit appears to be considerably more effective than stabilization of the B subunit. Our data suggest that these two distinct sites could cooperate in the reconstituted enzyme.

scholarly journals The C-terminal domain of DNA gyrase A adopts a DNA-bending  -pinwheel fold

2004 ◽  
Vol 101 (19) ◽  
pp. 7293-7298 ◽  
Author(s):  
K. D. Corbett ◽  
R. K. Shultzaberger ◽  
J. M. Berger
Keyword(s):  
Dna Bending ◽  
Dna Gyrase ◽  
Terminal Domain ◽  
Gyrase A

scholarly journals Glutamate racemase from Mycobacterium tuberculosis inhibits DNA gyrase by affecting its DNA-binding

2006 ◽  
Vol 34 (19) ◽  
pp. 5567-5576 ◽  
Author(s):  
Sugopa Sengupta ◽  
Meera Shah ◽  
Valakunja Nagaraja
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Dna Binding ◽  
Dna Gyrase ◽  
Glutamate Racemase

scholarly journals Functional Analysis of DNA Gyrase Mutant Enzymes Carrying Mutations at Position 88 in the A Subunit Found in Clinical Strains of Mycobacterium tuberculosis Resistant to Fluoroquinolones

2006 ◽  
Vol 50 (12) ◽  
pp. 4170-4173 ◽  
Author(s):  
Stéphanie Matrat ◽  
Nicolas Veziris ◽  
Claudine Mayer ◽  
Vincent Jarlier ◽  
Chantal Truffot-Pernot ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Dna Gyrase ◽  
Multidrug Resistant ◽  
Site Directed Mutagenesis ◽  
Fluoroquinolone Resistance ◽  
Directed Mutagenesis ◽  
The Novel ◽  
Wild Type ◽  
Clinical Strains ◽  
A Subunit

ABSTRACT We investigated the enzymatic efficiency and inhibition by quinolones of Mycobacterium tuberculosis DNA gyrases carrying the previously described GyrA G88C mutation and the novel GyrA G88A mutation harbored by two multidrug-resistant clinical strains and reproduced by site-directed mutagenesis. Fluoroquinolone MICs and 50% inhibitory concentrations for both mutants were 2- to 43-fold higher than for the wild type, demonstrating that these mutations confer fluoroquinolone resistance in M. tuberculosis.

scholarly journals Molecular analysis of lambda bio transducing phage produced by oxolinic acid-induced illegitimate recombination in vivo.

Genetics ◽  
1995 ◽  
Vol 140 (3) ◽  
pp. 889-896 ◽  
Author(s):  
H Shimizu ◽  
H Yamaguchi ◽  
H Ikeda
Keyword(s):  
Dna Gyrase ◽  
Oxolinic Acid ◽  
Illegitimate Recombination ◽  
Prophage Induction ◽  
Minority Class ◽  
E Coli ◽  
Gyrase A ◽  
A Subunit ◽  
Dependent Mechanism

Abstract To study the mechanism of DNA gyrase-mediated illegitimate recombination in Escherichia coli, we examined the formation of lambda Spi- phage during prophage induction. The frequency of Spi- phage was two to three orders of magnitude higher in the presence of oxolinic acid, an inhibitor of DNA gyrase A subunit, than in the absence of the drug, while it was very low in nalAr bacteria with the drug. RecA function is not required for the formation of these phages, indicating that this enhancement is not caused by the expression of SOS-controlled genes. Analyses of att region and recombination junctions of Spi- phages revealed that they have essentially the same structures as lambda bio transducing phages but are classified into two groups with respect to recombination sites. In the majority class of the transducing phages, there were not more than 3-bp homologies between the parental E. coli bio and lambda recombination sites. In the minority class of the transducing phages, on the other hand, 9-10-bp homologies were found between the parental recombination sites. These results suggested that oxolinic acid-induced illegitimate recombination takes place by two variants of a DNA gyrase-dependent mechanism.

scholarly journals Purification, crystallization and preliminary X-ray crystallographic studies of theMycobacterium tuberculosisDNA gyrase CTD

2012 ◽  
Vol 68 (2) ◽  
pp. 178-180 ◽  
Author(s):  
Amélie Darmon ◽  
Jérémie Piton ◽  
Mélanie Roué ◽  
Stéphanie Petrella ◽  
Alexandra Aubry ◽  
...  
Keyword(s):  
Unique Feature ◽  
Dna Gyrase ◽  
Type Ii ◽  
Asymmetric Unit ◽  
X Ray Diffraction ◽  
Unique Type ◽  
X Ray ◽  
His Tag ◽  
Gyrase A ◽  
A Subunit

Mycobacterium tuberculosisDNA gyrase, a nanomachine involved in regulation of DNA topology, is the only type II topoisomerase present in this organism and hence is the sole target of fluoroquinolone in the treatment of tuberculosis. The C-terminal domain (CTD) of the DNA gyrase A subunit possesses a unique feature, the ability to wrap DNA in a chiral manner, that plays an essential role during the catalytic cycle. A construct of 36 kDa corresponding to this domain has been overproduced, purified and crystallized. Diffraction data were collected to 1.55 Å resolution. Cleavage of the N-terminal His tag was crucial for obtaining crystals. The crystals belonged to space groupP212121, with one molecule in the asymmetric unit and a low solvent content (33%). This is the first report of the crystallization and preliminary X-ray diffraction studies of a DNA gyrase CTD from a species that contains one unique type II topoisomerase.

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